Search Results - "Tams, Jeppe W."

Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase by Tams, Jeppe W, Welinder, Karen G

“…The influence of N-linked glycans on the stability of glycoproteins has been studied using horseradish peroxidase isoenzyme C (HRP), which contains eight…”
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Structural and mechanistic studies of chloride induced activation of human pancreatic α‐amylase by Maurus, Robert, Begum, Anjuman, Kuo, Hsin‐Hen, Racaza, Andrew, Numao, Shin, Andersen, Carsten, Tams, Jeppe W., Vind, Jesper, Overall, Christopher M., Withers, Stephen G., Brayer, Gary D.

“…The mechanism of allosteric activation of α‐amylase by chloride has been studied through structural and kinetic experiments focusing on the chloride‐dependent…”
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Unfolding and Refolding of Coprinus cinereus Peroxidase at High pH, in Urea, and at High Temperature. Effect of Organic and Ionic Additives on These Processes by Tams, Jeppe W, Welinder, Karen G

“…The unfolding and refolding rates of the heme- and Ca2+-containing Coprinus cinereus peroxidase (CIP) have been measured at pH 12.1, in 4 M urea, and at 61.2…”
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Identification of pituitary adenylate cyclase-activating polypeptide1-38-binding factor in human plasma, as ceruloplasmin by TAMS, Jeppe W., JOHNSEN, Anders H., FAHRENKRUG, Jan

“…125I-Pituitary adenylate cyclase-activating polypeptide (PACAP) 1-38 is able to bind a factor in human plasma, which can be displaced by unlabelled PACAP 1-38…”
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Kinetic Stability of Designed Glycosylation Mutants of Coprinus cinereus Peroxidase by Tams, Jeppe W., Welinder, Karen G.

“…The effect of glycans and surface mutations on protein unfolding induced by heat or urea has been studied. Removal of the only native high mannose type glycan…”
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Mild Chemical Deglycosylation of Horseradish Peroxidase Yields a Fully Active, Homogeneous Enzyme by Tams, J.W., Welinder, K.G.

“…Horseradish peroxidase isoenzyme C (HRP) contains eight N-linked glycans composed of Man, Xyl, Fuc, and GlcNAc. These glycans were resistant to enzymatic…”
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Identification of pituitary adenylate cyclase-activating polypeptide1-38-binding factor in human plasma, as ceruloplasmin by Tams, J W, Johnsen, A H, Fahrenkrug, J

“…125I-Pituitary adenylate cyclase-activating polypeptide (PACAP) 1-38 is able to bind a factor in human plasma, which can be displaced by unlabelled PACAP 1-38…”
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Adapting protein solubility by glycosylation.: N-Glycosylation mutants of Coprinus cinereus peroxidase in salt and organic solutions by Tams, Jeppe W., Vind, Jesper, Welinder, Karen G.

“…Protein solubility is a fundamental parameter in biology and biotechnology. In the present study we have constructed and analyzed five mutants of Coprinus…”
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Crystallization and X-ray diffraction analysis of recombinant Coprinus cinereus peroxidase by Petersen, J F, Tams, J W, Vind, J, Svensson, A, Dalbøge, H, Welinder, K G, Larsen, S

“…Crystals suitable for an X-ray diffraction investigation have been obtained of recombinant Coprinus cinereus peroxidase expressed in Aspergillus oryzae. The…”
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Disulfide Bonds and Glycosylation in Fungal Peroxidases by Limongi, Paola, Kjalke, Marianne, Vind, Jesper, Tams, Jeppe W., Johansson, Tomas, Welinder, Karen G.

“…Four conserved disulfide bonds and N‐linked and O‐linked glycans of extracellular fungal peroxidases have been identified from studies of a lignin and a…”
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NMR studies of recombinant Coprinus peroxidase and three site‐directed mutants by VEITCH, Nigel C., TAMS, Jeppe W., VIND, Jesper, DALBØGE, Henrik, WELINDER, Karen G.

“…Proton nuclear magnetic resonance spectroscopy has been used to characterise and compare wild‐type fungal and recombinant Coprinus cinereus peroxidase (CIP)…”
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NMR studies of recombinant Coprinus peroxidase and three site-directed mutants. Implications for peroxidase substrate binding by Veitch, N.C, Tams, J.W, Vind, J, Dalboge, H, Welinder, K.G

“…Proton nuclear magnetic resonance spectroscopy has been used to characterise and compare wild-type fungal and recombinant Coprinus cinereus peroxidase (CIP)…”
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Adapting protein solubility by glycosylation by Tams, Jeppe W., Vind, Jesper, Welinder, Karen G.

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